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A6SUF7 (HEM1_JANMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase

Short name=GluTR
EC=1.2.1.70
Gene names
Name:hemA
Ordered Locus Names:mma_0214
OrganismJanthinobacterium sp. (strain Marseille) (Minibacterium massiliensis) [Complete proteome] [HAMAP]
Taxonomic identifier375286 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeJanthinobacterium

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00087

Domain

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335047

Regions

Nucleotide binding199 – 2046NADP By similarity
Region56 – 594Substrate binding By similarity
Region124 – 1263Substrate binding By similarity

Sites

Active site571Nucleophile By similarity
Binding site1191Substrate By similarity
Binding site1301Substrate By similarity
Site1091Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A6SUF7 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: B22847099D3678CE

FASTA42947,029
        10         20         30         40         50         60 
MQLLAVGLNH TTAPVSLREK VAFPADQLGQ AVASARSWYG RSDATTYTDE AAILSTCNRT 

        70         80         90        100        110        120 
ELYAASNLPG GVNEAIDITA HFLADYHKLP YAELRPYLYA LPQDNAVRHA FRVASGLDSM 

       130        140        150        160        170        180 
VLGEPQILGQ MKDAVRQAEA AGGLGTYLHQ MFQRTFAVAK EVRSTTEIGA HSVSMAAASV 

       190        200        210        220        230        240 
RLSQRIFDKI SEQNVLFIGA GEMIELSATH FAAQNPKSVT IANRTLERGQ TLAHRFNGKA 

       250        260        270        280        290        300 
IRLADLPDQL ASYDIVISST ASSLPIIGLG MVERAIKARR HKPMFMVDLA VPRDIEAEIG 

       310        320        330        340        350        360 
RLDDVFLYTV DDLGSFVQTG VENRQAAVAQ AEAIIETRVR SFMHWIDARA VVPVIQDLHE 

       370        380        390        400        410        420 
SSETMRMIEL ERARKLLAKG EDIDAVLEAL SKGLTAKFLH GPQQALNNAQ GDERARLAAL 


LPQLFRTKR 

« Hide

References

[1]"Genome analysis of Minibacterium massiliensis highlights the convergent evolution of water-living bacteria."
Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D., Drancourt M.
PLoS Genet. 3:1454-1463(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Marseille.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000269 Genomic DNA. Translation: ABR88801.1.
RefSeqYP_001351904.1. NC_009659.1.

3D structure databases

ProteinModelPortalA6SUF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375286.mma_0214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR88801; ABR88801; mma_0214.
GeneID5351794.
KEGGmms:mma_0214.
PATRIC22152829. VBIJanSp106498_0220.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycJSP375286:GJ8U-214-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_JANMA
AccessionPrimary (citable) accession number: A6SUF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways